Molecular analysis of VCA1008: a putative phosphoporin of Vibrio cholerae
The PhoB/PhoR-dependent response to inorganic phosphate (Pi)-starvation in Vibrio cholerae O1 includes the expression of vc0719 for the response regulator PhoB, vca0033 for an alkaline phosphatase and vca1008 for an outer membrane protein (OMP). Sequences with high identity to these genes have been...
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| Veröffentlicht in: | FEMS microbiology letters 2009-09, Vol.298 (2), p.241-248 |
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| creator | Goulart, Carolina L Lery, Letícia M.S Diniz, Michelle M.P Vianez-Junior, João L Neves-Ferreira, Ana Gisele C Perales, Jonas Bisch, Paulo M von Krüger, Wanda M.A |
| description | The PhoB/PhoR-dependent response to inorganic phosphate (Pi)-starvation in Vibrio cholerae O1 includes the expression of vc0719 for the response regulator PhoB, vca0033 for an alkaline phosphatase and vca1008 for an outer membrane protein (OMP). Sequences with high identity to these genes have been found in the genome of clinical and environmental strains, suggesting that the Pi-starvation response in V. cholerae is well conserved. VCA1008, an uncharacterized OMP involved in V. cholerae pathogenicity, presents sequence similarity to porins of Gram-negative bacteria such as phosphoporin PhoE from Escherichia coli. A three-dimensional model shows that VCA1008 is a 16-stranded pore-forming β-barrel protein that shares three of the four conserved lysine residues responsible for PhoE anionic specificity with PhoE. VCA1008 β-barrel apparently forms trimers that collapse into monomers by heating. Properties such as heat modifiability and resistance to denaturation by sodium dodecyl sulfate at lower temperatures permitted us to suggest that VCA1008 is a classical porin, more precisely, a phosphoporin due to its Pi starvation-induced PhoB-dependent expression, demonstrated by electrophoretic mobility shift assay and promoter fusion-lacZ assays. |
| doi_str_mv | 10.1111/j.1574-6968.2009.01727.x |
| format | Article |
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Sequences with high identity to these genes have been found in the genome of clinical and environmental strains, suggesting that the Pi-starvation response in V. cholerae is well conserved. VCA1008, an uncharacterized OMP involved in V. cholerae pathogenicity, presents sequence similarity to porins of Gram-negative bacteria such as phosphoporin PhoE from Escherichia coli. A three-dimensional model shows that VCA1008 is a 16-stranded pore-forming β-barrel protein that shares three of the four conserved lysine residues responsible for PhoE anionic specificity with PhoE. VCA1008 β-barrel apparently forms trimers that collapse into monomers by heating. Properties such as heat modifiability and resistance to denaturation by sodium dodecyl sulfate at lower temperatures permitted us to suggest that VCA1008 is a classical porin, more precisely, a phosphoporin due to its Pi starvation-induced PhoB-dependent expression, demonstrated by electrophoretic mobility shift assay and promoter fusion-lacZ assays.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2009.01727.x</identifier><identifier>PMID: 19659744</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>Alkaline phosphatase ; Amino Acid Sequence ; Artificial Gene Fusion ; Bacteria ; Bacterial Proteins - metabolism ; Bacteriology ; beta-Galactosidase - genetics ; beta-Galactosidase - metabolism ; Biological and medical sciences ; Coliforms ; Collapse ; Conserved sequence ; Denaturation ; DNA, Bacterial - metabolism ; E coli ; Electrophoretic mobility ; Electrophoretic Mobility Shift Assay ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Bacterial ; Gene sequencing ; Genes, Reporter ; Genomes ; Gram-negative bacteria ; Hot Temperature ; Low temperature ; Lysine ; Membrane proteins ; Microbiology ; Miscellaneous ; Models, Molecular ; Molecular Sequence Data ; Monomers ; outer membrane protein ; Outer membrane proteins ; Pathogenicity ; Pathogens ; Phosphates - metabolism ; phosphoporin ; Pore formation ; Porins ; Porins - chemistry ; Porins - genetics ; Porins - metabolism ; Protein Binding ; Protein Multimerization ; Protein Stability ; Protein Structure, Tertiary ; Proteins ; Sequence Homology, Amino Acid ; Sodium dodecyl sulfate ; Sodium lauryl sulfate ; Sulfate resistance ; Three dimensional models ; Trimers ; VCA1008 ; Vibrio cholerae ; Vibrio cholerae O1 - genetics ; Vibrio cholerae O1 - metabolism ; Waterborne diseases</subject><ispartof>FEMS microbiology letters, 2009-09, Vol.298 (2), p.241-248</ispartof><rights>2009 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved 2009</rights><rights>2009 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5257-f26335243669e2b3ed8feafbf1de10e69c0ff864491b6155639db5d69cb7438b3</citedby><cites>FETCH-LOGICAL-c5257-f26335243669e2b3ed8feafbf1de10e69c0ff864491b6155639db5d69cb7438b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.2009.01727.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2009.01727.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,781,785,1418,27929,27930,45579,45580</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21829788$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19659744$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Goulart, Carolina L</creatorcontrib><creatorcontrib>Lery, Letícia M.S</creatorcontrib><creatorcontrib>Diniz, Michelle M.P</creatorcontrib><creatorcontrib>Vianez-Junior, João L</creatorcontrib><creatorcontrib>Neves-Ferreira, Ana Gisele C</creatorcontrib><creatorcontrib>Perales, Jonas</creatorcontrib><creatorcontrib>Bisch, Paulo M</creatorcontrib><creatorcontrib>von Krüger, Wanda M.A</creatorcontrib><title>Molecular analysis of VCA1008: a putative phosphoporin of Vibrio cholerae</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>The PhoB/PhoR-dependent response to inorganic phosphate (Pi)-starvation in Vibrio cholerae O1 includes the expression of vc0719 for the response regulator PhoB, vca0033 for an alkaline phosphatase and vca1008 for an outer membrane protein (OMP). Sequences with high identity to these genes have been found in the genome of clinical and environmental strains, suggesting that the Pi-starvation response in V. cholerae is well conserved. VCA1008, an uncharacterized OMP involved in V. cholerae pathogenicity, presents sequence similarity to porins of Gram-negative bacteria such as phosphoporin PhoE from Escherichia coli. A three-dimensional model shows that VCA1008 is a 16-stranded pore-forming β-barrel protein that shares three of the four conserved lysine residues responsible for PhoE anionic specificity with PhoE. VCA1008 β-barrel apparently forms trimers that collapse into monomers by heating. Properties such as heat modifiability and resistance to denaturation by sodium dodecyl sulfate at lower temperatures permitted us to suggest that VCA1008 is a classical porin, more precisely, a phosphoporin due to its Pi starvation-induced PhoB-dependent expression, demonstrated by electrophoretic mobility shift assay and promoter fusion-lacZ assays.</description><subject>Alkaline phosphatase</subject><subject>Amino Acid Sequence</subject><subject>Artificial Gene Fusion</subject><subject>Bacteria</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>beta-Galactosidase - genetics</subject><subject>beta-Galactosidase - metabolism</subject><subject>Biological and medical sciences</subject><subject>Coliforms</subject><subject>Collapse</subject><subject>Conserved sequence</subject><subject>Denaturation</subject><subject>DNA, Bacterial - metabolism</subject><subject>E coli</subject><subject>Electrophoretic mobility</subject><subject>Electrophoretic Mobility Shift Assay</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Gene sequencing</subject><subject>Genes, Reporter</subject><subject>Genomes</subject><subject>Gram-negative bacteria</subject><subject>Hot Temperature</subject><subject>Low temperature</subject><subject>Lysine</subject><subject>Membrane proteins</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Monomers</subject><subject>outer membrane protein</subject><subject>Outer membrane proteins</subject><subject>Pathogenicity</subject><subject>Pathogens</subject><subject>Phosphates - metabolism</subject><subject>phosphoporin</subject><subject>Pore formation</subject><subject>Porins</subject><subject>Porins - chemistry</subject><subject>Porins - genetics</subject><subject>Porins - metabolism</subject><subject>Protein Binding</subject><subject>Protein Multimerization</subject><subject>Protein Stability</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sodium dodecyl sulfate</subject><subject>Sodium lauryl sulfate</subject><subject>Sulfate resistance</subject><subject>Three dimensional models</subject><subject>Trimers</subject><subject>VCA1008</subject><subject>Vibrio cholerae</subject><subject>Vibrio cholerae O1 - genetics</subject><subject>Vibrio cholerae O1 - metabolism</subject><subject>Waterborne diseases</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkV1rFDEYhYNY7Fr9Czog1asZ33wnQi_KYm1hixdab0NmJrGzzG7GZEe7_95MZ6kgKgZCQvKc5HAOQgWGCufxdl1hLlkptFAVAdAVYElkdfcILR4uHqMFUKlKDFoeo6cprQGAERBP0DHWgmvJ2AJdXYfeNWNvY2G3tt-nLhXBF1-W5xhAvStsMYw7u-u-u2K4DSnPIcRue890dexC0dzmF6J1z9CRt31yzw_rCbq5eP95eVmuPn64Wp6vyoYTLktPBKWcMCqEdqSmrlXeWV973DoMTugGvFeCMY1rgTkXVLc1b_N5LRlVNT1Bb-Z3hxi-jS7tzKZLjet7u3VhTEZSNqWhZCZf_5MkIDXnmmXw1W_gOowxx5EZCoKwbIJmSs1UE0NK0XkzxG5j495gMFMtZm2m9M2UvplqMfe1mLssfXH4YKw3rv0lPPSQgdMDYFNjex_ttunSA0ewIloqlbmzmfvR9W7_3wbMxfVq2mU9nfVhHP6iLv9k_-Ws8jYY-zVmZzefCGAKWAjFtKA_Af9Tvhc</recordid><startdate>200909</startdate><enddate>200909</enddate><creator>Goulart, Carolina L</creator><creator>Lery, Letícia M.S</creator><creator>Diniz, Michelle M.P</creator><creator>Vianez-Junior, João L</creator><creator>Neves-Ferreira, Ana Gisele C</creator><creator>Perales, Jonas</creator><creator>Bisch, Paulo M</creator><creator>von Krüger, Wanda M.A</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><general>Wiley-Blackwell</general><general>Oxford University Press</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>F1W</scope><scope>H95</scope><scope>H97</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>200909</creationdate><title>Molecular analysis of VCA1008: a putative phosphoporin of Vibrio cholerae</title><author>Goulart, Carolina L ; Lery, Letícia M.S ; Diniz, Michelle M.P ; Vianez-Junior, João L ; Neves-Ferreira, Ana Gisele C ; Perales, Jonas ; Bisch, Paulo M ; von Krüger, Wanda M.A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5257-f26335243669e2b3ed8feafbf1de10e69c0ff864491b6155639db5d69cb7438b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Alkaline phosphatase</topic><topic>Amino Acid Sequence</topic><topic>Artificial Gene Fusion</topic><topic>Bacteria</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>beta-Galactosidase - genetics</topic><topic>beta-Galactosidase - metabolism</topic><topic>Biological and medical sciences</topic><topic>Coliforms</topic><topic>Collapse</topic><topic>Conserved sequence</topic><topic>Denaturation</topic><topic>DNA, Bacterial - metabolism</topic><topic>E coli</topic><topic>Electrophoretic mobility</topic><topic>Electrophoretic Mobility Shift Assay</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Gene sequencing</topic><topic>Genes, Reporter</topic><topic>Genomes</topic><topic>Gram-negative bacteria</topic><topic>Hot Temperature</topic><topic>Low temperature</topic><topic>Lysine</topic><topic>Membrane proteins</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Monomers</topic><topic>outer membrane protein</topic><topic>Outer membrane proteins</topic><topic>Pathogenicity</topic><topic>Pathogens</topic><topic>Phosphates - metabolism</topic><topic>phosphoporin</topic><topic>Pore formation</topic><topic>Porins</topic><topic>Porins - chemistry</topic><topic>Porins - genetics</topic><topic>Porins - metabolism</topic><topic>Protein Binding</topic><topic>Protein Multimerization</topic><topic>Protein Stability</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sodium dodecyl sulfate</topic><topic>Sodium lauryl sulfate</topic><topic>Sulfate resistance</topic><topic>Three dimensional models</topic><topic>Trimers</topic><topic>VCA1008</topic><topic>Vibrio cholerae</topic><topic>Vibrio cholerae O1 - genetics</topic><topic>Vibrio cholerae O1 - metabolism</topic><topic>Waterborne diseases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Goulart, Carolina L</creatorcontrib><creatorcontrib>Lery, Letícia M.S</creatorcontrib><creatorcontrib>Diniz, Michelle M.P</creatorcontrib><creatorcontrib>Vianez-Junior, João L</creatorcontrib><creatorcontrib>Neves-Ferreira, Ana Gisele C</creatorcontrib><creatorcontrib>Perales, Jonas</creatorcontrib><creatorcontrib>Bisch, Paulo M</creatorcontrib><creatorcontrib>von Krüger, Wanda M.A</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection (ProQuest)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - 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Sequences with high identity to these genes have been found in the genome of clinical and environmental strains, suggesting that the Pi-starvation response in V. cholerae is well conserved. VCA1008, an uncharacterized OMP involved in V. cholerae pathogenicity, presents sequence similarity to porins of Gram-negative bacteria such as phosphoporin PhoE from Escherichia coli. A three-dimensional model shows that VCA1008 is a 16-stranded pore-forming β-barrel protein that shares three of the four conserved lysine residues responsible for PhoE anionic specificity with PhoE. VCA1008 β-barrel apparently forms trimers that collapse into monomers by heating. Properties such as heat modifiability and resistance to denaturation by sodium dodecyl sulfate at lower temperatures permitted us to suggest that VCA1008 is a classical porin, more precisely, a phosphoporin due to its Pi starvation-induced PhoB-dependent expression, demonstrated by electrophoretic mobility shift assay and promoter fusion-lacZ assays.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>19659744</pmid><doi>10.1111/j.1574-6968.2009.01727.x</doi><tpages>8</tpages></addata></record> |
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| subjects | Alkaline phosphatase Amino Acid Sequence Artificial Gene Fusion Bacteria Bacterial Proteins - metabolism Bacteriology beta-Galactosidase - genetics beta-Galactosidase - metabolism Biological and medical sciences Coliforms Collapse Conserved sequence Denaturation DNA, Bacterial - metabolism E coli Electrophoretic mobility Electrophoretic Mobility Shift Assay Escherichia coli Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Bacterial Gene sequencing Genes, Reporter Genomes Gram-negative bacteria Hot Temperature Low temperature Lysine Membrane proteins Microbiology Miscellaneous Models, Molecular Molecular Sequence Data Monomers outer membrane protein Outer membrane proteins Pathogenicity Pathogens Phosphates - metabolism phosphoporin Pore formation Porins Porins - chemistry Porins - genetics Porins - metabolism Protein Binding Protein Multimerization Protein Stability Protein Structure, Tertiary Proteins Sequence Homology, Amino Acid Sodium dodecyl sulfate Sodium lauryl sulfate Sulfate resistance Three dimensional models Trimers VCA1008 Vibrio cholerae Vibrio cholerae O1 - genetics Vibrio cholerae O1 - metabolism Waterborne diseases |
| title | Molecular analysis of VCA1008: a putative phosphoporin of Vibrio cholerae |
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